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  • Female  (143)
  • Base Sequence  (124)
  • Mutation  (61)
  • American Association for the Advancement of Science (AAAS)  (295)
  • American Association for the Advancement of Science
  • American Institute of Physics (AIP)
  • 1985-1989  (237)
  • 1975-1979  (58)
  • 1950-1954
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  • American Association for the Advancement of Science (AAAS)  (295)
  • American Association for the Advancement of Science
  • American Institute of Physics (AIP)
  • Springer  (6)
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  • 1
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    The MHC-binding and gp120-binding functions of CD4 are separable (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-08-18
    Description: CD4 is a cell surface glycoprotein that is thought to interact with nonpolymorphic determinants of class II major histocompatibility (MHC) molecules. CD4 is also the receptor for the human immunodeficiency virus (HIV), binding with high affinity to the HIV-1 envelope glycoprotein, gp120. Homolog-scanning mutagenesis was used to identify CD4 regions that are important in class II MHC binding and to determine whether the gp120 and class II MHC binding sites of CD4 are related. Class II MHC binding was abolished by mutations in each of the first three immunoglobulin-like domains of CD4. The gp120 binding could be abolished without affecting class II MHC binding and vice versa, although at least one mutation examined reduced both functions significantly. These findings indicate that, while there may be overlap between the gp120 and class II MHC binding sites of CD4, these sites are distinct and can be separated. Thus it should be possible to design CD4 analogs that can block HIV infectivity but intrinsically lack the ability to affect the normal immune response by binding to class II MHC molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lamarre, D -- Ashkenazi, A -- Fleury, S -- Smith, D H -- Sekaly, R P -- Capon, D J -- New York, N.Y. -- Science. 1989 Aug 18;245(4919):743-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire d'Immunologie, Institut de Recherches Cliniques de Montreal, Quebec, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2549633" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Surface ; Binding Sites ; DNA, Recombinant ; HIV/*metabolism ; HIV Envelope Protein gp120 ; HLA-DP Antigens/immunology ; Histocompatibility Antigens Class II/*immunology ; Humans ; Hybridomas ; Mice ; Molecular Sequence Data ; Mutation ; Receptors, HIV ; Receptors, Virus/genetics/immunology/*metabolism ; Retroviridae Proteins/immunology/*metabolism ; Rosette Formation ; Structure-Activity Relationship ; T-Lymphocytes/immunology/metabolism ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Identification of a thyroid hormone receptor that is pituitary-specific (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-04-07
    Description: Three cellular homologs of the v-erbA oncogene were previously identified in the rat; two of them encode high affinity receptors for the thyroid hormone triiodothyronine (T3). A rat complementary DNA clone encoding a T3 receptor form of the ErbA protein, called r-ErbA beta-2, was isolated. The r-ErbA beta-2 protein differs at its amino terminus from the previously described rat protein encoded by c-erbA beta and referred to as r-ErbA beta-1. Unlike the other members of the c-erbA proto-oncogene family, which have a wide tissue distribution, r-erbA beta-2 appears to be expressed only in the anterior pituitary gland. In addition, thyroid hormone downregulates r-erbA beta-2 messenger RNA but not r-erbA beta-1 messenger RNA in a pituitary tumor-derived cell line. The presence of a pituitary-specific form of the thyroid hormone receptor that may be selectively regulated by thyroid hormone could be important for the differential regulation of gene expression by T3 in the pituitary gland.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hodin, R A -- Lazar, M A -- Wintman, B I -- Darling, D S -- Koenig, R J -- Larsen, P R -- Moore, D D -- Chin, W W -- New York, N.Y. -- Science. 1989 Apr 7;244(4900):76-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Brigham and Women's Hospital, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2539642" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Cloning, Molecular ; DNA/isolation & purification ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Organ Specificity ; Pituitary Gland, Anterior/*metabolism ; Proto-Oncogene Proteins/genetics/*isolation & purification ; Rats ; Receptors, Thyroid Hormone/genetics/*isolation & purification ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    The 35-nucleotide spliced leader sequence is common to all trypanosome messenger RNA's (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-08-01
    Description: In Trypanosomatidae the messenger RNA's (mRNA's) that code for the variant surface glycoproteins (VSG's), tubulins, calmodulin, and at least a subset of other proteins contain a common 35-nucleotide leader sequence at their 5' ends. Hybrid-arrested in vitro translation has been used to show that all mRNA's in both African and South American trypanosomes contain this 35-nucleotide sequence. Oligonucleotides complementary to this sequence blocked translation of all trypanosome mRNA's in a rabbit reticulocyte lysate system, but did not inhibit translation of mRNA's from other organisms lacking this sequence. An oligonucleotide complementary to the VSG mRNA downstream from the spliced leader sequence arrested only VSG synthesis. Thus, the 35-nucleotide leader sequence is a general feature of all trypanosome mRNA's. The high specificity of oligonucleotides complementary to the spliced leader for their target sequence suggests that analogues permeable to the cell membrane may be useful in the treatment of trypanosomal infections.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Walder, J A -- Eder, P S -- Engman, D M -- Brentano, S T -- Walder, R Y -- Knutzon, D S -- Dorfman, D M -- Donelson, J E -- AI-18954/AI/NIAID NIH HHS/ -- AM-25295/AM/NIADDK NIH HHS/ -- HL-33555/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Aug 1;233(4763):569-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3523758" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Protein Biosynthesis ; Protein Sorting Signals/*genetics ; RNA, Messenger/*genetics ; Trypanosoma/*genetics ; Trypanosoma brucei brucei/genetics ; Trypanosoma cruzi/genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    A mammalian mitochondrial RNA processing activity contains nucleus-encoded RNA (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-03-06
    Description: Ribonuclease mitochondrial RNA processing, a site-specific endoribonuclease involved in primer RNA metabolism in mammalian mitochondria, requires an RNA component for its activity. On the basis of copurification and selective inactivation with complementary oligonucleotides, a 135-nucleotide RNA species, not encoded in the mitochondrial genome, is identified as the RNA moiety of the endoribonuclease. This finding implies transport of a nucleus-encoded RNA, essential for organelle DNA replication, to the mitochondrial matrix.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, D D -- Clayton, D A -- GM-33088-16/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Mar 6;235(4793):1178-84.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2434997" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Nucleus/*physiology ; Chemical Phenomena ; Chemistry ; Drug Resistance ; Endonucleases/isolation & purification/metabolism ; Enzyme Activation/drug effects ; *Genetic Code ; Humans ; Mammals/*genetics/metabolism ; Micrococcal Nuclease/pharmacology ; Mitochondria/*metabolism ; Oligonucleotides/pharmacology ; Organoids/physiology ; RNA/*biosynthesis/genetics/isolation & purification/physiology ; Ribonucleases/metabolism ; Subcellular Fractions/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Identification of human uromodulin as the Tamm-Horsfall urinary glycoprotein (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-04-03
    Description: The primary structure of human uromodulin, a 616-amino acid, 85-kilodalton glycoprotein with in vitro immunosuppressive properties, was determined through isolation and characterization of complementary DNA and genomic clones. The amino acid sequence encoded by one of the exons of the uromodulin gene has homology to the low-density-lipoprotein receptor and the epidermal growth factor precursor. Northern hybridization analyses demonstrate that uromodulin is synthesized by the kidney. Evidence is provided that uromodulin is identical to the previously characterized Tamm-Horsfall glycoprotein, the most abundant protein in normal human urine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennica, D -- Kohr, W J -- Kuang, W J -- Glaister, D -- Aggarwal, B B -- Chen, E Y -- Goeddel, D V -- New York, N.Y. -- Science. 1987 Apr 3;236(4797):83-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3453112" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/analysis ; Base Sequence ; Chemistry, Physical ; Cloning, Molecular ; Cysteine ; DNA/genetics ; Gene Expression Regulation ; Genes ; Glycoproteins/*genetics ; Humans ; Mucoproteins/*analysis/*genetics ; Peptide Fragments/analysis ; Physicochemical Phenomena ; RNA, Messenger/genetics ; Uromodulin
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    T-cell receptor beta-chain expression: dependence on relatively few variable region genes (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-08-09
    Description: Fifteen independently isolated complementary DNA clones that contain T-cell receptor (TCR) V beta genes were sequenced and found to represent 11 different V beta genes. When compared with known sequences, 14 different V beta genes could be defined from a total of 25 complementary DNA's; 11 clones therefore involved repeated usage of previously identified V beta's. Based on these data, we calculate a maximum likelihood estimate of the number of expressed germline V beta genes to be 18 with an upper 95 percent confidence bound of 30 genes. Southern blot analysis has shown that most of these genes belong to single element subfamilies which show very limited interstrain polymorphism. The TCR beta-chain diversity appears to be generated from a limited V beta gene pool primarily by extensive variability at the variable-diversity-joining (V-D-J) junctional site, with no evidence for the involvement of somatic hypermutation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Behlke, M A -- Spinella, D G -- Chou, H S -- Sha, W -- Hartl, D L -- Loh, D Y -- GM07200/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Aug 9;229(4713):566-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3875151" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Base Sequence ; Chromosome Mapping ; Cloning, Molecular ; Dna ; Gene Pool ; *Genetic Variation ; Humans ; Hybridomas ; Immunoglobulin Variable Region/genetics ; Mice ; Mice, Inbred BALB C/genetics ; Mice, Inbred C57BL/genetics ; Mice, Inbred Strains/genetics ; Receptors, Antigen, T-Cell/*genetics ; Species Specificity ; Spleen ; T-Lymphocytes ; Thymus Gland
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Atrial natriuretic peptide elevation in congestive heart failure in the human (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-03-07
    Description: A sensitive radioimmunoassay for atrial natriuretic peptide was used to examine the relation between circulating atrial natriuretic peptide and cardiac filling pressure in normal human subjects, in patients with cardiovascular disease and normal cardiac filling pressure, and in patients with cardiovascular disease and elevated cardiac filling pressure with and without congestive heart failure. The present studies establish a normal range for atrial natriuretic peptide in normal human subjects. These studies also establish that elevated cardiac filling pressure is associated with increased circulating concentrations of atrial natriuretic peptide and that congestive heart failure is not characterized by a deficiency in atrial natriuretic peptide, but with its elevation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Burnett, J C Jr -- Kao, P C -- Hu, D C -- Heser, D W -- Heublein, D -- Granger, J P -- Opgenorth, T J -- Reeder, G S -- New York, N.Y. -- Science. 1986 Mar 7;231(4742):1145-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2935937" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Atrial Natriuretic Factor/*blood ; Cardiovascular Diseases/blood ; Female ; Heart Failure/*blood ; Hemodynamics ; Humans ; Male ; Middle Aged ; Radioimmunoassay
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Studies of the human c-myb gene and its product in human acute leukemias (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-07-18
    Description: The myb gene is the transforming oncogene of the avian myeloblastosis virus (AMV); its normal cellular homolog, c-myb, is conserved across a broad span of evolution. In humans, c-myb is expressed in malignant hematopoietic cell lines and in primary hematopoietic tumors. Partial complementary DNA clones were generated from blast cells of patients with acute myelogenous leukemia. The sequences of the clones were compared to the c-myb of other species, as well as the v-myb of AMV. In addition, the carboxyl terminal region of human c-myb was placed in an expression vector to obtain protein for the generation of antiserum, which was used to identify the human c-myb gene product. Like v-myb, this protein was found within the nucleus of leukemic cells where it was associated with the nuclear matrix. These studies provide further evidence that c-myb might be involved in human leukemia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Slamon, D J -- Boone, T C -- Murdock, D C -- Keith, D E -- Press, M F -- Larson, R A -- Souza, L M -- CA36827/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1986 Jul 18;233(4761):347-51.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3014652" target="_blank"〉PubMed〈/a〉
    Keywords: *Aspartate Carbamoyltransferase ; Avian Leukosis Virus/*genetics ; Avian Myeloblastosis Virus/*genetics ; Base Sequence ; *Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing) ; Cell Line ; Cloning, Molecular ; DNA/analysis ; DNA Restriction Enzymes/metabolism ; *Dihydroorotase ; Escherichia coli/genetics ; Hematopoietic Stem Cells/microbiology ; Humans ; Leukemia, Myeloid, Acute/*genetics ; Molecular Weight ; *Multienzyme Complexes ; *Oncogenes ; Proteins/analysis
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    Gene for von Recklinghausen neurofibromatosis is in the pericentromeric region of chromosome 17 (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-05-29
    Description: Linkage analysis of 15 Utah kindreds demonstrated that a gene responsible for von Recklinghausen neurofibromatosis (NF) is located near the centromere on chromosome 17. The families also gave no evidence for heterogeneity, indicating that a significant proportion of NF cases are due to mutations at a single locus. Further genetic analysis can now refine this localization and may lead to the eventual identification and cloning of the defective gene responsible for this disorder.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barker, D -- Wright, E -- Nguyen, K -- Cannon, L -- Fain, P -- Goldgar, D -- Bishop, D T -- Carey, J -- Baty, B -- Kivlin, J -- CA 28854/CA/NCI NIH HHS/ -- CA 36362/CA/NCI NIH HHS/ -- GM 29090/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 May 29;236(4805):1100-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3107130" target="_blank"〉PubMed〈/a〉
    Keywords: Centromere ; Chromosome Mapping ; *Chromosomes, Human, Pair 17/ultrastructure ; DNA, Recombinant ; Female ; *Genes ; Genetic Linkage ; Humans ; Male ; Neurofibromatosis 1/*genetics ; Nucleic Acid Hybridization
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Effects on Trichinella spiralis of host responses to purified antigens (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-02-22
    Description: Purification of two antigens (48-kilodalton polypeptide and a group with major subunits of 50 and 55 kilodaltons) from the infective larvae of the parasitic nematode Trichinella spiralis was recently reported. Immunization of mice with either of these antigens induces strong resistance to a subsequent challenge infection. In the study reported here the mechanism of this resistance was investigated by monitoring the parasite's life cycle in mice immunized with the antigens. Immunized mice were able to expel intestinal adult worms and to inhibit the fecundity of adult female worms at an accelerated rate compared to control mice. Accelerated expulsion and inhibition of fecundity may account entirely for the level of resistance induced by immunization. Although the effects of the immune response apparently are exerted on adult worms, the target antigens are expressed only by developing larvae. This suggests that immune effector mechanisms act on intestinal larvae in such a way that they develop into defective adults.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Silberstein, D S -- Despommier, D D -- New York, N.Y. -- Science. 1985 Feb 22;227(4689):948-50.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3969571" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Helminth/immunology/*isolation & purification ; Female ; Immunization ; Larva ; Male ; Mice ; Trichinella/growth & development/*immunology ; Trichinellosis/immunology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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